ID   HTPG_WOLTR              Reviewed;         637 AA.
AC   Q5GTE5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=Wbm0138;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(2005).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR   EMBL; AE017321; AAW70729.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5GTE5; -.
DR   SMR; Q5GTE5; -.
DR   STRING; 292805.Wbm0138; -.
DR   EnsemblBacteria; AAW70729; AAW70729; Wbm0138.
DR   KEGG; wbm:Wbm0138; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000534; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224236"
FT   REGION          1..338
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          339..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          493..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..637
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   637 AA;  72410 MW;  99443D9A5D835B8F CRC64;
     MMELKMHNVK GTENLKFDAE VGKVLNIVIH SLYTNKDIFL RELVSNASDA CDKLRYESQL
     NPNLLDSSGE LKITISSNKD ENELYVTDNG IGMSRQDLIG NLGTIASSGT QKFLDAIKNS
     KDSSQAVELI GKFGVGFYSS FMVASEVIVE SRKAGEEESW VWRSTGDGEY SISKLDNQIP
     CGTKITLVMR PEENEFLDKF RIENIVTTYS DHINFPVEFI DEEGKSEKLN SKAAIWTKLK
     NDVTQEEHND FFRGVAHVGG EPWMILHNKN EGAIEYTNLL YVPSIKPFDL FHPDRRCSVK
     LYVNKVFITE DNVQIIPQYL RFLKGVVDSP DLPLNISRET LQNNRVVEQI RKSLTKRVIS
     ELGKKAKENL EEYTKFWTNF GAVLKEGLCE AMPTEEREAL LSICRFHSTG DKKLVSIDDY
     ISRMKPEQGY IYYLTGNSLD SVKNSPQLEG FISKGLEVLL FVDPVDDFWT SVIHEYKGQK
     FKSVTRADVD LEKFSPEEKD KENKSDEERA EGNTDSILQY FTKVLGNAVK SVKISKKLTD
     SPVCLAVDEG AMDLRMERFL REQNQLNYRT PKVLEVNTKH SVIKSIIKSY AENGENPTLE
     DMVHLLFYQA CIVEGEEMDD ASLFAKKLNN LLGKVII